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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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BAK1

Introduction

BCL2-antagonist/killer 1, also known as BAK1, is a human gene.

The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress.[1]

References

References

  1. ↑ “Entrez Gene: BAK1 BCL2-antagonist/killer 1”.
Further reading

Further reading

  • Buytaert E, Callewaert G, Vandenheede JR, Agostinis P (2007). “Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum”. Autophagy. 2 (3): 238–40. PMID 16874066.
  • Farrow SN, White JH, Martinou I; et al. (1995). “Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K”. Nature. 374 (6524): 731–3. doi:10.1038/374731a0. PMID 7715729.
  • Chittenden T, Harrington EA, O’Connor R; et al. (1995). “Induction of apoptosis by the Bcl-2 homologue Bak”. Nature. 374 (6524): 733–6. doi:10.1038/374733a0. PMID 7715730.
  • Kiefer MC, Brauer MJ, Powers VC; et al. (1995). “Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak”. Nature. 374 (6524): 736–9. doi:10.1038/374736a0. PMID 7715731.
  • Chittenden T, Flemington C, Houghton AB; et al. (1996). “A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions”. EMBO J. 14 (22): 5589–96. PMID 8521816.
  • Sattler M, Liang H, Nettesheim D; et al. (1997). “Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis”. Science. 275 (5302): 983–6. PMID 9020082.
  • Diaz JL, Oltersdorf T, Horne W; et al. (1997). “A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members”. J. Biol. Chem. 272 (17): 11350–5. PMID 9111042.
  • Huang DC, Adams JM, Cory S (1998). “The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4”. EMBO J. 17 (4): 1029–39. doi:10.1093/emboj/17.4.1029. PMID 9463381.
  • Herberg JA, Phillips S, Beck S; et al. (1998). “Genomic structure and domain organisation of the human Bak gene”. Gene. 211 (1): 87–94. PMID 9573342.
  • Narita M, Shimizu S, Ito T; et al. (1999). “Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria”. Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14681–6. PMID 9843949.
  • Song Q, Kuang Y, Dixit VM, Vincenz C (1999). “Boo, a novel negative regulator of cell death, interacts with Apaf-1”. EMBO J. 18 (1): 167–78. doi:10.1093/emboj/18.1.167. PMID 9878060.
  • Griffiths GJ, Dubrez L, Morgan CP; et al. (1999). “Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis”. J. Cell Biol. 144 (5): 903–14. PMID 10085290.
  • Shimizu S, Narita M, Tsujimoto Y (1999). “Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC”. Nature. 399 (6735): 483–7. doi:10.1038/20959. PMID 10365962.
  • Ohi N, Tokunaga A, Tsunoda H; et al. (1999). “A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region”. Cell Death Differ. 6 (4): 314–25. doi:10.1038/sj.cdd.4400493. PMID 10381623.
  • Holmgreen SP, Huang DC, Adams JM, Cory S (1999). “Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members”. Cell Death Differ. 6 (6): 525–32. doi:10.1038/sj.cdd.4400519. PMID 10381646.
  • Leo CP, Hsu SY, Chun SY; et al. (1999). “Characterization of the antiapoptotic Bcl-2 family member myeloid cell leukemia-1 (Mcl-1) and the stimulation of its message by gonadotropins in the rat ovary”. Endocrinology. 140 (12): 5469–77. PMID 10579309.
  • Shimizu S, Tsujimoto Y (2000). “Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity”. Proc. Natl. Acad. Sci. U.S.A. 97 (2): 577–82. PMID 10639121.
  • Bae J, Leo CP, Hsu SY, Hsueh AJ (2000). “MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain”. J. Biol. Chem. 275 (33): 25255–61. doi:10.1074/jbc.M909826199. PMID 10837489.
  • Wei MC, Lindsten T, Mootha VK; et al. (2000). “tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.”. Genes Dev. 14 (16): 2060–71. PMID 10950869.
  • Degterev A, Lugovskoy A, Cardone M; et al. (2001). “Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL”. Nat. Cell Biol. 3 (2): 173–82. PMID 11175750.

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